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2fqy

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[[Image:2fqy.gif|left|200px]]<br /><applet load="2fqy" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2fqy, resolution 1.90&Aring;" />
 
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'''PnrA from Treponema pallidum complexed with adenosine.'''<br />
 
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==Overview==
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==PnrA from Treponema pallidum complexed with adenosine.==
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Treponema pallidum, the bacterial agent of syphilis, cannot be cultivated in vitro. This constraint has severely impeded the study of the membrane biology of this complex human pathogen. A structure-to-function approach thus was adopted as a means of discerning the likely function of Tp0319, a 35-kDa cytoplasmic membrane-associated lipoprotein of T. pallidum formerly designated as TmpC. A 1.7-A crystal structure showed that recombinant Tp0319 (rTp0319) consists of two alpha/beta domains, linked by three crossovers, with a deep cleft between them akin to ATP-binding cassette (ABC) receptors. In the cleft, a molecule of inosine was bound. Isothermal titration calorimetry demonstrated that rTp0319 specifically binds purine nucleosides (dissociation constant (Kd) approximately 10(-7) M). This predilection for purine nucleosides by rTp0319 is consistent with its likely role as a receptor component of a cytoplasmic membrane-associated transporter system. Reverse transcription-PCR analysis of RNA isolated from rabbit tissue-extracted T. pallidum additionally showed that tp0319 is transcriptionally linked to four other downstream open reading frames, thereby supporting the existence of an ABC-like operon (tp0319-0323). We herein thus re-name tp0319 as purine nucleoside receptor A (pnrA), with its operonic partners tp0320-0323 designated as pnrB-E, respectively. Our study not only infers that PnrA transports purine nucleosides essential for the survival of T. pallidum within its obligate human host, but to our knowledge, this is the first description of an ABC-type nucleoside transport system in any bacterium. PnrA has been grouped with a functionally uncharacterized protein family (HBG016869), thereby implying that other members of the family may have similar nucleoside-binding function(s).
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<StructureSection load='2fqy' size='340' side='right'caption='[[2fqy]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[2fqy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Treponema_pallidum Treponema pallidum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FQY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FQY FirstGlance]. <br>
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2FQY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Treponema_pallidum Treponema pallidum] with <scene name='pdbligand=ADN:'>ADN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FQY OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fqy OCA], [https://pdbe.org/2fqy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fqy RCSB], [https://www.ebi.ac.uk/pdbsum/2fqy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fqy ProSAT]</span></td></tr>
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The PnrA (Tp0319; TmpC) lipoprotein represents a new family of bacterial purine nucleoside receptor encoded within an ATP-binding cassette (ABC)-like operon in Treponema pallidum., Deka RK, Brautigam CA, Yang XF, Blevins JS, Machius M, Tomchick DR, Norgard MV, J Biol Chem. 2006 Mar 24;281(12):8072-81. Epub 2006 Jan 16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16418175 16418175]
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</table>
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[[Category: Single protein]]
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== Function ==
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[https://www.uniprot.org/uniprot/TMPC_TREPA TMPC_TREPA] Binds purine nucleosides and may play a role in purine nucleoside uptake. May be part of an ABC-type nucleoside uptake system. Has highest affinity for guanosine, followed by inosine and adenosine. Has very low affinity for cytidine and does not bind thymidine.<ref>PMID:16418175</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fq/2fqy_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2fqy ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Treponema pallidum]]
[[Category: Treponema pallidum]]
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[[Category: Brautigam, C A.]]
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[[Category: Brautigam CA]]
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[[Category: Deka, R K.]]
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[[Category: Deka RK]]
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[[Category: Machius, M.]]
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[[Category: Machius M]]
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[[Category: Norgard, M V.]]
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[[Category: Norgard MV]]
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[[Category: Tomchick, D R.]]
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[[Category: Tomchick DR]]
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[[Category: ADN]]
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[[Category: abc receptor protein]]
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[[Category: nucleoside binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:24:15 2008''
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Current revision

PnrA from Treponema pallidum complexed with adenosine.

PDB ID 2fqy

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